HEADER LIGASE 02-FEB-10 3LN6
TITLE CRYSTAL STRUCTURE OF A BIFUNCTIONAL GLUTATHIONE SYNTHETASE FROM
TITLE 2 STREPTOCOCCUS AGALACTIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE BIOSYNTHESIS BIFUNCTIONAL PROTEIN GSHAB;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GAMMA-GCS-GS, GCS-GS, GLUTAMATE-CYSTEINE LIGASE, GAMMA-
COMPND 5 GLUTAMYLCYSTEINE SYNTHETASE, GAMMA-ECS, GCS, GLUTATHIONE SYNTHETASE,
COMPND 6 GLUTATHIONE SYNTHASE, GSH SYNTHETASE, GSH-S, GSHASE, GS;
COMPND 7 EC: 6.3.2.2, 6.3.2.3;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS AGALACTIAE SEROGROUP V;
SOURCE 3 ORGANISM_TAXID: 216466;
SOURCE 4 STRAIN: BAA-811;
SOURCE 5 GENE: GSHAB, GSHF, SAG1821;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS GAMMA-GLUTAMYL CYSTEINE LIGASE DOMAIN, ATP-GRASP DOMAIN, HYBRID
KEYWDS 2 ENZYME, ATP-BINDING, GLUTATHIONE BIOSYNTHESIS, LIGASE, MAGNESIUM,
KEYWDS 3 MANGANESE, METAL-BINDING, MULTIFUNCTIONAL ENZYME, NUCLEOTIDE-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.STOUT,B.VERGAUWEN,S.N.SAVVIDES
REVDAT 1 13-APR-11 3LN6 0
JRNL AUTH J.STOUT,D.DE VOS,B.VERGAUWEN,S.N.SAVVIDES
JRNL TITL STRUCTURES OF TWO BIFUNCTIONAL GAMMA-GLUTAMATE-CYSTEINE
JRNL TITL 2 LIGASE/GLUTATHIONE SYNTHETASES (GSHF) REVEAL A NOVEL HYBRID
JRNL TITL 3 ATP-GRASP FOLD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23309
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1178
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 4.6700 - 4.0800 0.01 0 145 0.2070 0.2600
REMARK 3 2 4.0800 - 3.7100 0.01 0 148 0.2470 0.3160
REMARK 3 3 3.7100 - 3.4500 0.01 0 142 0.2740 0.2730
REMARK 3 4 3.4500 - 3.2500 0.01 0 142 0.3000 0.3550
REMARK 3 5 3.2500 - 3.0800 0.01 0 145 0.3220 0.4180
REMARK 3 6 3.0800 - 2.9500 0.01 0 153 0.3530 0.4280
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 76.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 95.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.03000
REMARK 3 B22 (A**2) : -1.03000
REMARK 3 B33 (A**2) : 2.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.014 NULL
REMARK 3 ANGLE : 1.512 NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MLHL MAXIMUM LIKELIHOOD REFINEMENT
REMARK 3 PROCEDURE
REMARK 4
REMARK 4 3LN6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB057484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-07; 12-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG; ESRF
REMARK 200 BEAMLINE : BW7A; ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0720; 0.9330
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM; ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24531
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 8.10
REMARK 200 R MERGE FOR SHELL (I) : 0.13200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS, MR
REMARK 200 SOFTWARE USED: SOLVE, MOLREP, PHASER
REMARK 200 STARTING MODEL: 1V4G, 1UC8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M (NH4)2SO4, 100MM TRIS-HCL PH 8.5,
REMARK 280 12% GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 71.51000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 71.51000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.61500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 71.51000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.80750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 71.51000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 158.42250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 71.51000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 158.42250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.51000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 52.80750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 71.51000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 71.51000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 105.61500
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 71.51000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 71.51000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 105.61500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 71.51000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 158.42250
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 71.51000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 52.80750
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 71.51000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 52.80750
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 71.51000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 158.42250
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 71.51000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 71.51000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 105.61500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 61850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 143.02000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 785 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 ILE A 3
REMARK 465 LEU A 250
REMARK 465 ILE A 251
REMARK 465 SER A 314
REMARK 465 SER A 315
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 9 CD NE CZ NH1 NH2
REMARK 470 HIS A 13 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 16 CD1
REMARK 470 ILE A 30 CD1
REMARK 470 GLN A 35 CG CD OE1 NE2
REMARK 470 ARG A 36 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 37 CG1 CG2
REMARK 470 THR A 40 OG1 CG2
REMARK 470 LYS A 44 CG CD CE NZ
REMARK 470 TYR A 59 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A 67 CD1
REMARK 470 ILE A 70 CD1
REMARK 470 VAL A 107 CG1 CG2
REMARK 470 ARG A 108 NE CZ NH1 NH2
REMARK 470 GLU A 109 CG CD OE1 OE2
REMARK 470 GLU A 110 CG CD OE1 OE2
REMARK 470 ASP A 111 CG OD1 OD2
REMARK 470 ILE A 112 CD1
REMARK 470 ILE A 114 CG1 CG2 CD1
REMARK 470 LEU A 117 CG CD1 CD2
REMARK 470 PHE A 121 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 122 CG CD OE1 OE2
REMARK 470 TYR A 123 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 124 CG OD1 OD2
REMARK 470 TYR A 125 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 126 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 127 CG CD CE NZ
REMARK 470 TYR A 128 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 130 CG CD OE1 OE2
REMARK 470 LYS A 131 CG CD CE NZ
REMARK 470 THR A 132 OG1 CG2
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 LEU A 136 CG CD1 CD2
REMARK 470 ILE A 137 CD1
REMARK 470 ILE A 140 CD1
REMARK 470 GLU A 152 CD OE1 OE2
REMARK 470 LEU A 160 CG CD1 CD2
REMARK 470 ILE A 167 CD1
REMARK 470 ASP A 168 CG OD1 OD2
REMARK 470 LYS A 176 CD CE NZ
REMARK 470 ARG A 183 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 202 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 204 CG OD1 OD2
REMARK 470 GLN A 205 CD OE1 NE2
REMARK 470 LYS A 206 CG CD CE NZ
REMARK 470 LEU A 207 CG CD1 CD2
REMARK 470 VAL A 211 CG1 CG2
REMARK 470 LEU A 214 CG CD1 CD2
REMARK 470 SER A 217 OG
REMARK 470 VAL A 222 CG1 CG2
REMARK 470 ASN A 223 CG OD1
REMARK 470 HIS A 224 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 ASP A 226 CG OD1 OD2
REMARK 470 ILE A 227 CD1
REMARK 470 ARG A 228 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 229 CD1
REMARK 470 SER A 230 OG
REMARK 470 TYR A 231 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 234 CG CD1 CD2
REMARK 470 LYS A 235 CG CD CE NZ
REMARK 470 VAL A 238 CG1 CG2
REMARK 470 ASN A 239 CG OD1
REMARK 470 LEU A 241 CG CD1 CD2
REMARK 470 ASN A 243 CG OD1
REMARK 470 LYS A 246 CE NZ
REMARK 470 SER A 247 OG
REMARK 470 GLU A 253 CG CD OE1 OE2
REMARK 470 LYS A 254 CG CD CE NZ
REMARK 470 GLU A 255 CG CD OE1 OE2
REMARK 470 ARG A 261 NE CZ NH1 NH2
REMARK 470 ARG A 269 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 270 CG OD1
REMARK 470 TYR A 271 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 272 CG CD1 CD2
REMARK 470 GLU A 273 CG CD OE1 OE2
REMARK 470 LYS A 274 CG CD CE NZ
REMARK 470 ILE A 276 CD1
REMARK 470 ILE A 292 CD1
REMARK 470 LEU A 304 CG CD1 CD2
REMARK 470 ILE A 312 CG1 CG2 CD1
REMARK 470 ASP A 313 CG OD1 OD2
REMARK 470 SER A 316 OG
REMARK 470 ILE A 318 CG1 CG2 CD1
REMARK 470 ASP A 319 CG OD1 OD2
REMARK 470 GLN A 320 CG CD OE1 NE2
REMARK 470 ASP A 321 CG OD1 OD2
REMARK 470 ILE A 322 CG1 CG2 CD1
REMARK 470 LYS A 323 CG CD CE NZ
REMARK 470 GLU A 324 CG CD OE1 OE2
REMARK 470 ARG A 327 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 331 CG CD1 CD2
REMARK 470 ILE A 332 CG1 CG2 CD1
REMARK 470 SER A 335 OG
REMARK 470 LEU A 338 CG CD1 CD2
REMARK 470 GLU A 339 CG CD OE1 OE2
REMARK 470 LEU A 341 CG CD1 CD2
REMARK 470 GLN A 359 CG CD OE1 NE2
REMARK 470 ASN A 362 CG OD1
REMARK 470 SER A 364 OG
REMARK 470 ARG A 376 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 378 CG1 CG2 CD1
REMARK 470 GLU A 382 CG CD OE1 OE2
REMARK 470 MET A 392 SD CE
REMARK 470 ILE A 393 CD1
REMARK 470 LEU A 396 CG CD1 CD2
REMARK 470 LYS A 440 CD CE NZ
REMARK 470 VAL A 446 CG1 CG2
REMARK 470 GLN A 450 CD OE1 NE2
REMARK 470 SER A 460 OG
REMARK 470 ILE A 462 CD1
REMARK 470 LYS A 473 CD CE NZ
REMARK 470 ILE A 477 CD1
REMARK 470 LYS A 485 CG CD CE NZ
REMARK 470 ILE A 491 CG1 CG2 CD1
REMARK 470 PHE A 505 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 507 CG OD1 OD2
REMARK 470 ARG A 508 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 509 CE NZ
REMARK 470 ASN A 513 CG OD1
REMARK 470 PHE A 515 CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 517 CD OE1 NE2
REMARK 470 ILE A 518 CG1 CG2 CD1
REMARK 470 GLN A 519 CG CD OE1 NE2
REMARK 470 LYS A 521 NZ
REMARK 470 ILE A 523 CD1
REMARK 470 LYS A 526 CE NZ
REMARK 470 LYS A 528 CG CD CE NZ
REMARK 470 SER A 529 OG
REMARK 470 THR A 530 OG1 CG2
REMARK 470 ASN A 531 CG OD1
REMARK 470 LEU A 534 CG CD1 CD2
REMARK 470 ILE A 536 CG1 CG2 CD1
REMARK 470 ILE A 538 CD1
REMARK 470 PHE A 539 CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 544 CG OD1
REMARK 470 LEU A 545 CG CD1 CD2
REMARK 470 GLU A 549 CG CD OE1 OE2
REMARK 470 LYS A 550 CG CD CE NZ
REMARK 470 ILE A 552 CD1
REMARK 470 ILE A 554 CD1
REMARK 470 THR A 557 OG1 CG2
REMARK 470 GLU A 558 CG CD OE1 OE2
REMARK 470 ILE A 562 CG1 CG2 CD1
REMARK 470 ILE A 583 CD1
REMARK 470 ASP A 596 CG OD1 OD2
REMARK 470 ILE A 598 CG1 CG2 CD1
REMARK 470 TYR A 616 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 617 CG OD1 OD2
REMARK 470 ILE A 625 CD1
REMARK 470 GLU A 629 CG CD OE1 OE2
REMARK 470 GLU A 648 CG CD OE1 OE2
REMARK 470 LYS A 651 CD CE NZ
REMARK 470 ILE A 652 CD1
REMARK 470 ARG A 656 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 660 CD1
REMARK 470 ILE A 698 CD1
REMARK 470 SER A 707 OG
REMARK 470 LYS A 708 CG CD CE NZ
REMARK 470 ASP A 709 CG OD1 OD2
REMARK 470 LYS A 710 CG CD CE NZ
REMARK 470 LYS A 711 CG CD CE NZ
REMARK 470 ILE A 716 CD1
REMARK 470 MET A 726 SD CE
REMARK 470 LEU A 750 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 693 CB CYS A 693 SG -0.125
REMARK 500 CYS A 730 CB CYS A 730 SG -0.099
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 288 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 48 142.57 -37.17
REMARK 500 TYR A 59 -61.20 -138.46
REMARK 500 PRO A 69 176.27 -53.22
REMARK 500 ASN A 209 177.49 95.56
REMARK 500 ARG A 269 -21.66 92.08
REMARK 500 LEU A 286 137.86 -37.20
REMARK 500 ILE A 312 32.64 -80.56
REMARK 500 GLU A 449 -55.72 77.32
REMARK 500 ASN A 459 -127.99 63.42
REMARK 500 LYS A 485 -58.37 75.36
REMARK 500 GLN A 519 -65.86 -128.78
REMARK 500 ASN A 531 -154.10 -74.58
REMARK 500 GLU A 579 -125.05 48.98
REMARK 500 CYS A 693 163.17 -48.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 751
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LN7 RELATED DB: PDB
DBREF 3LN6 A 1 750 UNP Q8DXM9 GSHAB_STRA5 1 750
SEQRES 1 A 750 MET ILE ILE ASP ARG LEU LEU GLN ARG SER HIS SER HIS
SEQRES 2 A 750 LEU PRO ILE LEU GLN ALA THR PHE GLY LEU GLU ARG GLU
SEQRES 3 A 750 SER LEU ARG ILE HIS GLN PRO THR GLN ARG VAL ALA GLN
SEQRES 4 A 750 THR PRO HIS PRO LYS THR LEU GLY SER ARG ASN TYR HIS
SEQRES 5 A 750 PRO TYR ILE GLN THR ASP TYR SER GLU PRO GLN LEU GLU
SEQRES 6 A 750 LEU ILE THR PRO ILE ALA LYS ASP SER GLN GLU ALA ILE
SEQRES 7 A 750 ARG PHE LEU LYS ALA ILE SER ASP VAL ALA GLY ARG SER
SEQRES 8 A 750 ILE ASN HIS ASP GLU TYR LEU TRP PRO LEU SER MET PRO
SEQRES 9 A 750 PRO LYS VAL ARG GLU GLU ASP ILE GLN ILE ALA GLN LEU
SEQRES 10 A 750 GLU ASP ALA PHE GLU TYR ASP TYR ARG LYS TYR LEU GLU
SEQRES 11 A 750 LYS THR TYR GLY LYS LEU ILE GLN SER ILE SER GLY ILE
SEQRES 12 A 750 HIS TYR ASN LEU GLY LEU GLY GLN GLU LEU LEU THR SER
SEQRES 13 A 750 LEU PHE GLU LEU SER GLN ALA ASP ASN ALA ILE ASP PHE
SEQRES 14 A 750 GLN ASN GLN LEU TYR MET LYS LEU SER GLN ASN PHE LEU
SEQRES 15 A 750 ARG TYR ARG TRP LEU LEU THR TYR LEU TYR GLY ALA SER
SEQRES 16 A 750 PRO VAL ALA GLU GLU ASP PHE LEU ASP GLN LYS LEU ASN
SEQRES 17 A 750 ASN PRO VAL ARG SER LEU ARG ASN SER HIS LEU GLY TYR
SEQRES 18 A 750 VAL ASN HIS LYS ASP ILE ARG ILE SER TYR THR SER LEU
SEQRES 19 A 750 LYS ASP TYR VAL ASN ASP LEU GLU ASN ALA VAL LYS SER
SEQRES 20 A 750 GLY GLN LEU ILE ALA GLU LYS GLU PHE TYR SER PRO VAL
SEQRES 21 A 750 ARG LEU ARG GLY SER LYS ALA CYS ARG ASN TYR LEU GLU
SEQRES 22 A 750 LYS GLY ILE THR TYR LEU GLU PHE ARG THR PHE ASP LEU
SEQRES 23 A 750 ASN PRO PHE SER PRO ILE GLY ILE THR GLN GLU THR VAL
SEQRES 24 A 750 ASP THR VAL HIS LEU PHE LEU LEU ALA LEU LEU TRP ILE
SEQRES 25 A 750 ASP SER SER SER HIS ILE ASP GLN ASP ILE LYS GLU ALA
SEQRES 26 A 750 ASN ARG LEU ASN ASP LEU ILE ALA LEU SER HIS PRO LEU
SEQRES 27 A 750 GLU LYS LEU PRO ASN GLN ALA PRO VAL SER ASP LEU VAL
SEQRES 28 A 750 ASP ALA MET GLN SER VAL ILE GLN HIS PHE ASN LEU SER
SEQRES 29 A 750 PRO TYR TYR GLN ASP LEU LEU GLU SER VAL LYS ARG GLN
SEQRES 30 A 750 ILE GLN SER PRO GLU LEU THR VAL ALA GLY GLN LEU LEU
SEQRES 31 A 750 GLU MET ILE GLU GLY LEU SER LEU GLU THR PHE GLY GLN
SEQRES 32 A 750 ARG GLN GLY GLN ILE TYR HIS ASP TYR ALA TRP GLU ALA
SEQRES 33 A 750 PRO TYR ALA LEU LYS GLY TYR GLU THR MET GLU LEU SER
SEQRES 34 A 750 THR GLN LEU LEU LEU PHE ASP VAL ILE GLN LYS GLY VAL
SEQRES 35 A 750 ASN PHE GLU VAL LEU ASP GLU GLN ASP GLN PHE LEU LYS
SEQRES 36 A 750 LEU TRP HIS ASN SER HIS ILE GLU TYR VAL LYS ASN GLY
SEQRES 37 A 750 ASN MET THR SER LYS ASP ASN TYR ILE VAL PRO LEU ALA
SEQRES 38 A 750 MET ALA ASN LYS VAL VAL THR LYS LYS ILE LEU ASP GLU
SEQRES 39 A 750 LYS HIS PHE PRO THR PRO PHE GLY ASP GLU PHE THR ASP
SEQRES 40 A 750 ARG LYS GLU ALA LEU ASN TYR PHE SER GLN ILE GLN ASP
SEQRES 41 A 750 LYS PRO ILE VAL VAL LYS PRO LYS SER THR ASN PHE GLY
SEQRES 42 A 750 LEU GLY ILE SER ILE PHE LYS THR SER ALA ASN LEU ALA
SEQRES 43 A 750 SER TYR GLU LYS ALA ILE ASP ILE ALA PHE THR GLU ASP
SEQRES 44 A 750 SER ALA ILE LEU VAL GLU GLU TYR ILE GLU GLY THR GLU
SEQRES 45 A 750 TYR ARG PHE PHE VAL LEU GLU GLY ASP CYS ILE ALA VAL
SEQRES 46 A 750 LEU LEU ARG VAL ALA ALA ASN VAL VAL GLY ASP GLY ILE
SEQRES 47 A 750 HIS THR ILE SER GLN LEU VAL LYS LEU LYS ASN GLN ASN
SEQRES 48 A 750 PRO LEU ARG GLY TYR ASP HIS ARG SER PRO LEU GLU VAL
SEQRES 49 A 750 ILE GLU LEU GLY GLU VAL GLU GLN LEU MET LEU GLU GLN
SEQRES 50 A 750 GLN GLY TYR THR VAL ASN SER ILE PRO PRO GLU GLY THR
SEQRES 51 A 750 LYS ILE GLU LEU ARG ARG ASN SER ASN ILE SER THR GLY
SEQRES 52 A 750 GLY ASP SER ILE ASP VAL THR ASN THR MET ASP PRO THR
SEQRES 53 A 750 TYR LYS GLN LEU ALA ALA GLU MET ALA GLU ALA MET GLY
SEQRES 54 A 750 ALA TRP VAL CYS GLY VAL ASP LEU ILE ILE PRO ASN ALA
SEQRES 55 A 750 THR GLN ALA TYR SER LYS ASP LYS LYS ASN ALA THR CYS
SEQRES 56 A 750 ILE GLU LEU ASN PHE ASN PRO LEU MET TYR MET HIS THR
SEQRES 57 A 750 TYR CYS GLN GLU GLY PRO GLY GLN SER ILE THR PRO ARG
SEQRES 58 A 750 ILE LEU ALA LYS LEU PHE PRO GLU LEU
HET SO4 A 751 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *35(H2 O)
HELIX 1 1 LEU A 6 SER A 10 5 5
HELIX 2 2 ASP A 73 ILE A 92 1 20
HELIX 3 3 ASP A 119 GLY A 134 1 16
HELIX 4 4 LYS A 135 ILE A 140 5 6
HELIX 5 5 GLY A 150 GLN A 162 1 13
HELIX 6 6 ASN A 165 TYR A 192 1 28
HELIX 7 7 SER A 233 ALA A 244 1 12
HELIX 8 8 ALA A 252 PHE A 256 5 5
HELIX 9 9 THR A 295 ILE A 312 1 18
HELIX 10 10 HIS A 317 SER A 335 1 19
HELIX 11 11 PRO A 346 ASN A 362 1 17
HELIX 12 12 SER A 364 SER A 380 1 17
HELIX 13 13 PRO A 381 LEU A 383 5 3
HELIX 14 14 THR A 384 ILE A 393 1 10
HELIX 15 15 LEU A 398 TRP A 414 1 17
HELIX 16 16 LEU A 420 GLU A 424 5 5
HELIX 17 17 GLU A 427 GLY A 441 1 15
HELIX 18 18 TYR A 476 MET A 482 1 7
HELIX 19 19 LYS A 485 LYS A 495 1 11
HELIX 20 20 GLU A 510 ILE A 518 1 9
HELIX 21 21 ASN A 544 ASP A 559 1 16
HELIX 22 22 THR A 600 ASN A 609 1 10
HELIX 23 23 GLY A 628 GLN A 638 1 11
HELIX 24 24 ASP A 674 MET A 688 1 15
HELIX 25 25 MET A 724 TYR A 729 1 6
HELIX 26 26 ILE A 738 PHE A 747 1 10
SHEET 1 A 3 ARG A 36 VAL A 37 0
SHEET 2 A 3 ALA A 19 HIS A 31 -1 N HIS A 31 O ARG A 36
SHEET 3 A 3 GLU A 96 LEU A 98 -1 O TYR A 97 N ILE A 30
SHEET 1 B 6 ILE A 55 THR A 57 0
SHEET 2 B 6 GLN A 63 ILE A 67 -1 O GLU A 65 N GLN A 56
SHEET 3 B 6 ALA A 19 HIS A 31 -1 N SER A 27 O LEU A 64
SHEET 4 B 6 ILE A 143 LEU A 149 -1 O GLY A 148 N THR A 20
SHEET 5 B 6 TYR A 278 PHE A 281 -1 O PHE A 281 N TYR A 145
SHEET 6 B 6 VAL A 260 ARG A 263 -1 N ARG A 261 O GLU A 280
SHEET 1 C 3 ASN A 443 VAL A 446 0
SHEET 2 C 3 PHE A 453 HIS A 458 -1 O LYS A 455 N GLU A 445
SHEET 3 C 3 HIS A 461 LYS A 466 -1 O GLU A 463 N LEU A 456
SHEET 1 D 4 PHE A 505 THR A 506 0
SHEET 2 D 4 ALA A 561 GLU A 566 -1 O ILE A 562 N PHE A 505
SHEET 3 D 4 ILE A 523 PRO A 527 -1 N LYS A 526 O LEU A 563
SHEET 4 D 4 SER A 537 PHE A 539 -1 O SER A 537 N VAL A 525
SHEET 1 E 5 ASP A 665 ASP A 668 0
SHEET 2 E 5 ASP A 581 VAL A 589 -1 N LEU A 587 O ILE A 667
SHEET 3 E 5 THR A 571 LEU A 578 -1 N ARG A 574 O LEU A 586
SHEET 4 E 5 GLY A 694 ILE A 699 -1 O VAL A 695 N PHE A 575
SHEET 5 E 5 THR A 714 ASN A 719 -1 O ASN A 719 N GLY A 694
SHEET 1 F 2 ASN A 592 VAL A 594 0
SHEET 2 F 2 LYS A 651 GLU A 653 -1 O ILE A 652 N VAL A 593
SHEET 1 G 2 ARG A 614 GLY A 615 0
SHEET 2 G 2 LEU A 622 GLU A 623 1 O LEU A 622 N GLY A 615
SITE 1 AC1 5 ARG A 588 ASN A 659 ILE A 660 SER A 661
SITE 2 AC1 5 HOH A 776
CRYST1 143.020 143.020 211.230 90.00 90.00 90.00 I 41 2 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006992 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006992 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004734 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
